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MNase-seq analysis of the Methnocaldococcus jannaschii nucleoid reveals a general size-variable hypernucleosome architecture

ABSTRACT: In eukaryotes, histone paralogues form obligate heterodimers such as H3/H4 and H2A/H2B that assemble into octameric nucleosome particles. Archaeal histones are dimeric and assemble on DNA into ‘hypernucleosome’ particles of varying sizes with each dimer wrapping 30 bp of DNA. These are likely composed of canonical and variant histone paralogues, but the function of these variants is poorly understood. Here, we characterise the structure and function of the histone paralogue MJ1647 from Methanocaldococcus jannaschii that has a unique C-terminal extension that enables MJ1647 homo-tetramerisation. The accompanying paper solves the crystal structure of MJ1647, but this part of the study specifically uses MNase-seq methodology to explore the hypernucleosome protection landscape of the in vivo M. jannaschii nucleoid.

ORGANISM(S): Methanocaldococcus jannaschii

PROVIDER: GSE216101 | GEO | 2022/10/22

REPOSITORIES: GEO

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